2pjw: Difference between revisions
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==Overview== | ==Overview== | ||
The yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex | The yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex deliver ubiquitinated transmembrane proteins to the ESCRT endosomal-sorting pathway. The Vps27/Hse1 complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. We have solved the crystal structure of the core responsible for the assembly of the Vps27/Hse1 complex at 3.0 A resolution. The structure consists of two intertwined GAT domains, each consisting of two helices from one subunit and one from the other. The two GAT domains are connected by an antiparallel coiled coil, forming a 90 A-long barbell-like structure. This structure places the domains of Vps27 and Hse1 that recruit ubiquitinated cargo and deubiquitinating enzymes close to each other. Coarse-grained Monte Carlo simulations of the Vps27/Hse1 complex on a membrane show how the complex binds cooperatively to lipids and ubiquitinated membrane proteins and acts as a scaffold for ubiquitination reactions. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
The Vps27/Hse1 | The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting., Prag G, Watson H, Kim YC, Beach BM, Ghirlando R, Hummer G, Bonifacino JS, Hurley JH, Dev Cell. 2007 Jun;12(6):973-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17543868 17543868] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Hurley, J | [[Category: Hurley, J H.]] | ||
[[Category: Prag, G.]] | [[Category: Prag, G.]] | ||
[[Category: core complex]] | [[Category: core complex]] | ||
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[[Category: gat domain]] | [[Category: gat domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:14 2008'' | ||
Revision as of 19:30, 21 February 2008
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The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting
OverviewOverview
The yeast Vps27/Hse1 complex and the homologous mammalian Hrs/STAM complex deliver ubiquitinated transmembrane proteins to the ESCRT endosomal-sorting pathway. The Vps27/Hse1 complex directly binds to ubiquitinated transmembrane proteins and recruits both ubiquitin ligases and deubiquitinating enzymes. We have solved the crystal structure of the core responsible for the assembly of the Vps27/Hse1 complex at 3.0 A resolution. The structure consists of two intertwined GAT domains, each consisting of two helices from one subunit and one from the other. The two GAT domains are connected by an antiparallel coiled coil, forming a 90 A-long barbell-like structure. This structure places the domains of Vps27 and Hse1 that recruit ubiquitinated cargo and deubiquitinating enzymes close to each other. Coarse-grained Monte Carlo simulations of the Vps27/Hse1 complex on a membrane show how the complex binds cooperatively to lipids and ubiquitinated membrane proteins and acts as a scaffold for ubiquitination reactions.
About this StructureAbout this Structure
2PJW is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitin-dependent sorting., Prag G, Watson H, Kim YC, Beach BM, Ghirlando R, Hummer G, Bonifacino JS, Hurley JH, Dev Cell. 2007 Jun;12(6):973-86. PMID:17543868
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